Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture
Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were p...
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todo:paper_03257541_v48_n4_p274_Kuhar2023-10-03T15:24:23Z Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture Kuhar, F. Castiglia, V.C. Zamora, J.C. Cellulase Laccase Lipase Litter degradation Xylanase amino acid amylase cellulase glycosidase laccase manganese peroxidase nitrophenol pectin polygalacturonase proton transporting adenosine triphosphate synthase ribosome DNA RNA polymerase II triacylglycerol lipase xenobiotic agent xylan 1,4 beta xylosidase xylan endo 1,3 beta xylosidase amylase carbon cellulase culture medium fungal protein laccase manganese peroxidase peroxidase polygalacturonase triacylglycerol lipase agar medium Article Cantharellales decolorization enzyme activity fungal cell culture Geastrum Geastrum argentinum Geastrum morganii Geastrum papinuttii Geastrum plicatum litter decomposition mycelium nonhuman Basidiomycetes comparative study culture medium enzymology growth, development and aging metabolism species difference Amylases Basidiomycota Carbon Cellulase Culture Media Fungal Proteins Laccase Lipase Peroxidases Polygalacturonase Species Specificity Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were performed on isolates of four species of this genus, showing evidence of laccase, cellulase, pectinase, amylase and lipase activity and suggesting that a wide range of carbon sources can be exploited by these species. For the first time in this genus, quantitative assays verified manganese peroxidase activity (up to 0.6 mU/g) in 30-day old cultures, as well as laccase, β-glycosidase and β-xylosidase activities. © 2016 Asociación Argentina de Microbiología Fil:Castiglia, V.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03257541_v48_n4_p274_Kuhar |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Cellulase Laccase Lipase Litter degradation Xylanase amino acid amylase cellulase glycosidase laccase manganese peroxidase nitrophenol pectin polygalacturonase proton transporting adenosine triphosphate synthase ribosome DNA RNA polymerase II triacylglycerol lipase xenobiotic agent xylan 1,4 beta xylosidase xylan endo 1,3 beta xylosidase amylase carbon cellulase culture medium fungal protein laccase manganese peroxidase peroxidase polygalacturonase triacylglycerol lipase agar medium Article Cantharellales decolorization enzyme activity fungal cell culture Geastrum Geastrum argentinum Geastrum morganii Geastrum papinuttii Geastrum plicatum litter decomposition mycelium nonhuman Basidiomycetes comparative study culture medium enzymology growth, development and aging metabolism species difference Amylases Basidiomycota Carbon Cellulase Culture Media Fungal Proteins Laccase Lipase Peroxidases Polygalacturonase Species Specificity |
spellingShingle |
Cellulase Laccase Lipase Litter degradation Xylanase amino acid amylase cellulase glycosidase laccase manganese peroxidase nitrophenol pectin polygalacturonase proton transporting adenosine triphosphate synthase ribosome DNA RNA polymerase II triacylglycerol lipase xenobiotic agent xylan 1,4 beta xylosidase xylan endo 1,3 beta xylosidase amylase carbon cellulase culture medium fungal protein laccase manganese peroxidase peroxidase polygalacturonase triacylglycerol lipase agar medium Article Cantharellales decolorization enzyme activity fungal cell culture Geastrum Geastrum argentinum Geastrum morganii Geastrum papinuttii Geastrum plicatum litter decomposition mycelium nonhuman Basidiomycetes comparative study culture medium enzymology growth, development and aging metabolism species difference Amylases Basidiomycota Carbon Cellulase Culture Media Fungal Proteins Laccase Lipase Peroxidases Polygalacturonase Species Specificity Kuhar, F. Castiglia, V.C. Zamora, J.C. Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture |
topic_facet |
Cellulase Laccase Lipase Litter degradation Xylanase amino acid amylase cellulase glycosidase laccase manganese peroxidase nitrophenol pectin polygalacturonase proton transporting adenosine triphosphate synthase ribosome DNA RNA polymerase II triacylglycerol lipase xenobiotic agent xylan 1,4 beta xylosidase xylan endo 1,3 beta xylosidase amylase carbon cellulase culture medium fungal protein laccase manganese peroxidase peroxidase polygalacturonase triacylglycerol lipase agar medium Article Cantharellales decolorization enzyme activity fungal cell culture Geastrum Geastrum argentinum Geastrum morganii Geastrum papinuttii Geastrum plicatum litter decomposition mycelium nonhuman Basidiomycetes comparative study culture medium enzymology growth, development and aging metabolism species difference Amylases Basidiomycota Carbon Cellulase Culture Media Fungal Proteins Laccase Lipase Peroxidases Polygalacturonase Species Specificity |
description |
Knowledge regarding the enzymatic machinery of fungi is decisive to understand their ecological role. The species of the genus Geastrum are known to grow extremely slowly in pure culture, which makes it difficult to evaluate physiological parameters such as enzyme activity. Qualitative assays were performed on isolates of four species of this genus, showing evidence of laccase, cellulase, pectinase, amylase and lipase activity and suggesting that a wide range of carbon sources can be exploited by these species. For the first time in this genus, quantitative assays verified manganese peroxidase activity (up to 0.6 mU/g) in 30-day old cultures, as well as laccase, β-glycosidase and β-xylosidase activities. © 2016 Asociación Argentina de Microbiología |
format |
JOUR |
author |
Kuhar, F. Castiglia, V.C. Zamora, J.C. |
author_facet |
Kuhar, F. Castiglia, V.C. Zamora, J.C. |
author_sort |
Kuhar, F. |
title |
Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture |
title_short |
Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture |
title_full |
Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture |
title_fullStr |
Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture |
title_full_unstemmed |
Detection of manganese peroxidase and other exoenzymes in four isolates of Geastrum (Geastrales) in pure culture |
title_sort |
detection of manganese peroxidase and other exoenzymes in four isolates of geastrum (geastrales) in pure culture |
url |
http://hdl.handle.net/20.500.12110/paper_03257541_v48_n4_p274_Kuhar |
work_keys_str_mv |
AT kuharf detectionofmanganeseperoxidaseandotherexoenzymesinfourisolatesofgeastrumgeastralesinpureculture AT castigliavc detectionofmanganeseperoxidaseandotherexoenzymesinfourisolatesofgeastrumgeastralesinpureculture AT zamorajc detectionofmanganeseperoxidaseandotherexoenzymesinfourisolatesofgeastrumgeastralesinpureculture |
_version_ |
1782025881306267648 |